The Sec61 complex is the central component of the protein translocation apparatus of the endoplasmic reticulum (ER) membrane. The protein encoded by this gene and SEC63 protein are found to be associated with ribosome-free SEC61 complex. It is speculated that Sec61-Sec62-Sec63 may perform post-translational protein translocation into the ER. The Sec61-Sec62-Sec63 complex might also perform the backward transport of ER proteins that are subject to the ubiquitin-proteasome-dependent degradation

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout

Caeruloplasmin is a copper binding plasma glycoprotein consisting of a single polypeptide chain. It has a molecular weight of 132kDa and occurs in plasma at a concentration of 150-500 mg/L. Although the physiological functions of Caeruloplasmin are not fully understood it is implicated in a number of possible functions. 95% of plasma copper is bound to Caeruloplasmin, implying some involvement in copper transport. Caeruloplasmin has been described as both an oxidant and an antioxidant, its ex

Calcium plays an essential role in many biological processes. The calcium binding protein (CaBP) family shares much similarity to calmodulin. It has been shown that CaBP proteins can substitute functionally for, and probably augment the function of, calmodulin. Calcium binding proteins are a crucial part of calcium mediated cellular signal transduction in the central nervous system. There are several members of the family with varying expression patterns. CaBP1 and CaBP2 can be expressed as m

This gene encodes a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Members of this family are secreted or membrane-anchored proteins mainly found in cells associated with the immune system. The SRCR family is defined by a 100-110 amino acid SRCR domain, which may mediate protein-protein interaction and ligand binding. The encoded protein contains twelve SRCR domains, a transmembrane region and a cytoplasmic domain. Alternative splicing results in multiple transcript varian